y
Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.010G091200.1 |
Family | GH28 |
Protein Properties | Length: 409 Molecular Weight: 43879.2 Isoelectric Point: 7.0744 |
Chromosome | Chromosome/Scaffold: 10 Start: 14252186 End: 14253795 |
Description | Pectin lyase-like superfamily protein |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
GH28 | 54 | 385 | 0 |
KEACASVTPSTVVIPKGTYLLTKVNLEGPCKAPIEINVQGTIQAPADPSVFKDPNWVRFYSIENFKMSGGGIFDGQGSIAYEKNKDPHNRAFRSKLPVNI RFDFVTNALIQDITSKDSKLFHVNVFACKNITLERFKVEAPEDSPNTDGIHLGKSDGVNIIGCDIKTGDDCISIGDGTKNMNIKEITCGPGHGISIGSLG KFPNEEPVEGIKVSNCTITNTSNGARIKTWPGESPGIVTDIHFEDIIVNNVSSPILIDQKYCPWSKCKINEESKVKLSNISFKNIRGTSALPEAVKFICS GSSPCQNVELADIDIKHTGAEPATSQCLNVKP |
Full Sequence |
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Protein Sequence Length: 409 Download |
MAPHLDIVPS MFVLLLLFIS ASKVQSDALD VVAKFGAKAD GKTDLSKPFL DAWKEACASV 60 TPSTVVIPKG TYLLTKVNLE GPCKAPIEIN VQGTIQAPAD PSVFKDPNWV RFYSIENFKM 120 SGGGIFDGQG SIAYEKNKDP HNRAFRSKLP VNIRFDFVTN ALIQDITSKD SKLFHVNVFA 180 CKNITLERFK VEAPEDSPNT DGIHLGKSDG VNIIGCDIKT GDDCISIGDG TKNMNIKEIT 240 CGPGHGISIG SLGKFPNEEP VEGIKVSNCT ITNTSNGARI KTWPGESPGI VTDIHFEDII 300 VNNVSSPILI DQKYCPWSKC KINEESKVKL SNISFKNIRG TSALPEAVKF ICSGSSPCQN 360 VELADIDIKH TGAEPATSQC LNVKPITSGK LNPTPCSSPV PKTLSATA* 420 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02218 | PLN02218 | 5.0e-83 | 32 | 393 | 366 | + polygalacturonase ADPG | ||
PLN02155 | PLN02155 | 2.0e-100 | 10 | 396 | 390 | + polygalacturonase | ||
PLN02793 | PLN02793 | 2.0e-100 | 21 | 398 | 383 | + Probable polygalacturonase | ||
pfam00295 | Glyco_hydro_28 | 9.0e-114 | 57 | 384 | 328 | + Glycosyl hydrolases family 28. Glycosyl hydrolase family 28 includes polygalacturonase EC:3.2.1.15 as well as rhamnogalacturonase A(RGase A), EC:3.2.1.-. These enzymes is important in cell wall metabolism. | ||
PLN02188 | PLN02188 | 7.0e-125 | 12 | 396 | 395 | + polygalacturonase/glycoside hydrolase family protein |
Gene Ontology | |
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GO Term | Description |
GO:0004650 | polygalacturonase activity |
GO:0005975 | carbohydrate metabolic process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
GenBank | ADC53480.1 | 0 | 1 | 408 | 1 | 412 | polygalacturonase [Gossypium hirsutum] |
DDBJ | BAA89476.1 | 0 | 5 | 396 | 3 | 393 | polygalacturonase [Salix gilgiana] |
Swiss-Prot | Q39766 | 0 | 1 | 408 | 1 | 407 | PGLR_GOSBA RecName: Full=Polygalacturonase; Short=PG; AltName: Full=Pectinase; Flags: Precursor |
Swiss-Prot | Q39786 | 0 | 1 | 408 | 1 | 407 | PGLR_GOSHI RecName: Full=Polygalacturonase; Short=PG; AltName: Full=Pectinase; Flags: Precursor |
RefSeq | XP_002274125.1 | 0 | 23 | 397 | 21 | 395 | PREDICTED: hypothetical protein [Vitis vinifera] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 2iq7_G | 4e-17 | 54 | 383 | 15 | 331 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 2iq7_F | 4e-17 | 54 | 383 | 15 | 331 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 2iq7_E | 4e-17 | 54 | 383 | 15 | 331 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 2iq7_D | 4e-17 | 54 | 383 | 15 | 331 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |
PDB | 2iq7_C | 4e-17 | 54 | 383 | 15 | 331 | A Chain A, Crystal Structure Of The Polygalacturonase From Colletotrichum Lupini And Its Implications For The Interaction With Polygalacturonase- Inhibiting Proteins |